L Aminoacid Oxidase
Mostrando 1-8 de 8 artigos, teses e dissertações.
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1. AÃÃo antibacteriana antifÃngica e antiparasitÃria de veneno de serpentes do gÃnero Bothrops e suas fraÃÃes fosfolipase A2 e L-AminoÃcido oxidase / Antibacterial, antifungal and antiparasitary action of Bothrops venoms and their fractions phospholipase A2 and L-aminoacid oxidase
Snakes venoms contain biologically active substances primarily consisting of proteins (90-95%). Some of these present enzymatic activities, such as phospholipases A2 and the L-amino acid oxidases. In this study we verify the action of Bothrops leucurus (BleuTV) and Bothrops marajoensis (BmarTV) venoms, and fractions PLA2 (BleuPLA2 and BmarPLA2) and LAAO (Ble
IBICT - Instituto Brasileiro de Informação em Ciência e Tecnologia. Publicado em: 08/04/2009
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2. Structural and functional caracterization of L-aminoácido oxidases isolated from snake Bothrops venoms / Caracterização funcional e estrutural de L-aminoácido oxidases isoladas de venenos de serpentes do gênero Bothrops
The aim of this project was the isolation of three L-aminoacid oxidases from Bothrops jararaca, Bothrops moojeni and Bothrops pirajai snake venoms, respectively, in addition to their biochemical, enzymatic, pharmacological and toxicological characterization. They were named BjarLAAO-I, BmooLAAO-I and BpirLAAO-I, respectively, and their isolation involved two
Publicado em: 2008
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3. Caracterização funcional e estrutural de uma L-Aminoácido oxidace do veneno de Bothrops jararacussue avaliação da sua ação antitumoral, antiparasitária e bactericida / Functional and structural characterization of an L-aminoacid oxidace from Bothrops jararacussuvenom and the evaluation of its antitumoral, antiparasitic and bactericidal action
In this research we described the isolation and biochemical, structural and functional characterization of an L-amino acid oxidase from Bothrops jararacussu venom, named BjussuLAAO. The purification was carried out through three chromatography steps, using a molecular filtration on Sephadex G-75, followed by an affinity chromatography on Benzamidine-Sepharos
Publicado em: 2006
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4. Alkylamine-Dependent Amino-Acid Oxidation by Lysine Monooxygenase—Fragmented Substrate of Oxygenase
Lysine monooxygenase catalyzes the oxygenative decarboxylation of L-lysine and produces a corresponding acid amide. L-Alanine was inactive as substrate. However, when propylamine was present, oxidation, but not oxygenation, of alanine was demonstrated with the oxygenase. Alanine was converted to pyruvate, with the liberation of ammonia and hydrogen peroxide,
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5. The sequence of the gene for cytochrome c oxidase subunit I, a frameshift containing gene for cytochrome c oxidase subunit II and seven unassigned reading frames in Trypanosoma brucei mitochrondrial maxi-circle DNA.
A 9.2 kb segment of the maxi-circle of Trypanosoma brucei mitochondrial DNA contains the genes for cytochrome c oxidase subunits I and II (coxI and coxII) and seven Unassigned Reading Frames ("URFs"). The genes for coxI and coxII display considerable homology at the aminoacid level (38 and 25%, respectively) to the corresponding genes in fungal and mammalian
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6. Biochemical and Molecular Characterization of a Laccase from Marasmius quercophilus
The basidiomycete Marasmius quercophilus is commonly found during autumn on the decaying litter of the evergreen oak (Quercus ilex L.), a plant characteristic of Mediterranean forest. This white-rot fungus colonizes the leaf surface with rhizomorphs, causing a total bleaching of the leaf. In synthetic liquid media, this white-rot fungus has strong laccase ac
American Society for Microbiology.
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7. Expression of the Xylulose 5-Phosphate Phosphoketolase Gene, xpkA, from Lactobacillus pentosus MD363 Is Induced by Sugars That Are Fermented via the Phosphoketolase Pathway and Is Repressed by Glucose Mediated by CcpA and the Mannose Phosphoenolpyruvate Phosphotransferase System
Purification of xylulose 5-phosphate phosphoketolase (XpkA), the central enzyme of the phosphoketolase pathway (PKP) in lactic acid bacteria, and cloning and sequence analysis of the encoding gene, xpkA, from Lactobacillus pentosus MD363 are described. xpkA encodes a 788-amino-acid protein with a calculated mass of 88,705 Da. Expression of xpkA in Escherichi
American Society for Microbiology.
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8. Mitochondrial Translation of Saccharomyces cerevisiae COX2 mRNA Is Controlled by the Nucleotide Sequence Specifying the Pre-Cox2p Leader Peptide
The mitochondrial gene encoding yeast cytochrome oxidase subunit II (Cox2p) specifies a precursor protein with a 15-amino-acid leader peptide. Deletion of the entire leader peptide coding region is known to block Cox2p accumulation posttranscriptionally. Here, we examined in vivo the role of the pre-Cox2p leader peptide and the mRNA sequence that encodes it
American Society for Microbiology.